{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T16:16:54Z","timestamp":1774973814441,"version":"3.50.1"},"reference-count":26,"publisher":"International Union of Crystallography (IUCr)","issue":"1","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"published-print":{"date-parts":[[2015,1,1]]},"abstract":"<jats:p>Microbial degradation of the plant cell wall is a fundamental biological process with considerable industrial importance. Hydrolysis of recalcitrant polysaccharides is orchestrated by a large repertoire of carbohydrate-active enzymes that display a modular architecture in which a catalytic domain is connected<jats:italic>via<\/jats:italic>linker sequences to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates, thus potentiating catalysis. The genome of the most abundant ruminal cellulolytic bacterium,<jats:italic>Ruminococcus flavefaciens<\/jats:italic>strain FD-1, provides an opportunity to discover novel cellulosomal proteins involved in plant cell-wall deconstruction. It encodes a modular protein comprising a glycoside hydrolase family 9 catalytic module (GH9) linked to two unclassified tandemly repeated CBMs (termed CBM-<jats:italic>Rf<\/jats:italic>6A and CBM-<jats:italic>Rf<\/jats:italic>6B) and a C-terminal dockerin. The novel CBM-<jats:italic>Rf<\/jats:italic>6A from this protein has been crystallized and data were processed for the native and a selenomethionine derivative to 1.75 and 1.5\u2005\u00c5 resolution, respectively. The crystals belonged to orthorhombic and cubic space groups, respectively. The structure was solved by a single-wavelength anomalous dispersion experiment using the<jats:italic>CCP<\/jats:italic>4 program suite and<jats:italic>SHELXC<\/jats:italic>\/<jats:italic>D<\/jats:italic>\/<jats:italic>E<\/jats:italic>.<\/jats:p>","DOI":"10.1107\/s2053230x14025576","type":"journal-article","created":{"date-parts":[[2014,12,23]],"date-time":"2014-12-23T16:58:10Z","timestamp":1419353890000},"page":"45-48","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":2,"title":["Crystallization and preliminary crystallographic studies of a novel noncatalytic carbohydrate-binding module from the<i>Ruminococcus flavefaciens<\/i>cellulosome"],"prefix":"10.1107","volume":"71","author":[{"given":"Immacolata","family":"Venditto","sequence":"first","affiliation":[]},{"given":"Arun","family":"Goyal","sequence":"additional","affiliation":[]},{"given":"Andrew","family":"Thompson","sequence":"additional","affiliation":[]},{"given":"Luis M. 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